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HAMAP rule MF_01318

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General rule information [?]

Accession MF_01318
Dates 22-JUL-2003 (Created)
17-FEB-2023 (Last updated, Version 32)
Name Ribosomal_L1
Scope
Bacteria
Archaea
Plastid
Templates P0A7L0 (RL1_ECOLI); Q5SLP7 (RL1_THET8); P27150 (RL1_THETH); P54050 (RL1_METJA); O52704 (RL1_METTL); P35024 (RL1_SULAC): [Recover all]
case <OC:Bacteria> or <OG:Chloroplast>
Triggered by
end case

case <OC:Archaea>
Triggered by
end case


Propagated annotation [?]


Identifier, protein and gene names [?]

case <OC:Bacteria> and not <OC:Cyanobacteriota>
Identifier
RL1
Protein name
RecName: Full=50S ribosomal protein L1;
Gene name
rplA
else case <OC:Cyanobacteriota>
Identifier
RL1
Protein name
RecName: Full=50S ribosomal protein L1;
Gene name
rplA, rpl1
else case <OC:Archaea>
Identifier
RL1
Protein name
RecName: Full=50S ribosomal protein L1;
Gene name
rpl1
else case <OG:Chloroplast>
Identifier
RK1
Protein name
RecName: Full=50S ribosomal protein L1, chloroplastic;
Gene name
rpl1
end case

Comments [?]

case <OC:Bacteria>
Function Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release.
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
else case <OC:Archaea>
Function Binds directly to 23S rRNA. Probably involved in E site tRNA release.
Protein L1 is also a translational repressor protein, it controls the translation of its operon by binding to its mRNA.
end case
Subunit Part of the 50S ribosomal subunit.
case <OG:Chloroplast>
Function Binds directly to 23S rRNA. Might be involved in E site tRNA release.
Subcellular location Plastid, chloroplast.
end case
Similarity Belongs to the universal ribosomal protein uL1 family.

Keywords [?]

Ribonucleoprotein
Ribosomal protein
RNA-binding
rRNA-binding
case not <OG:Chloroplast>
Repressor
Translation regulation
tRNA-binding
end case

Gene Ontology [?]

GO:0019843; Molecular function: rRNA binding.
GO:0006412; Biological process: translation.
case <OG:Chloroplast>
GO:0009507; Cellular component: chloroplast.
end case

Cross-references [?]

Pfam PF00687; Ribosomal_L1; 1;
TIGRFAMs TIGR01169; RplA_bact; 1;
PROSITE PS01199; RIBOSOMAL_L1; 1;

Additional information [?]

Size range 209-253 amino acids
Related rules None
Fusion Nter: None; Cter: <Unknown>
Comments C-terminal fusion in MALP2, quite atypical in NEOSM. Some of the Rickettsiales are about 15 residues shorter at the N-terminus. L1 proteins from thermophilic organisms have an approximately 10-fold higher affinity for their binding sites on both 23S rRNA and mRNA than do their mesophilic counterparts, maybe helping to explain the ribosome's greater stability in thermophiles. See: PubMed=9746351; Kohrer C., Mayer C., Neumair O., Grobner P., Piendl W.; "Interaction of ribosomal L1 proteins from mesophilic and thermophilic Archaea and Bacteria with specific L1-binding sites on 23S rRNA and mRNA."; Eur. J. Biochem. 256:97-105(1998).


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